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InterPro: IPR012287 Homeodomain-related
Protein matches
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UniProtKB Matches: 62373 proteins |
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Accession
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IPR012287 Homeodomain-rel |
Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR009057 Homeodomain-like
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Children
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IPR000005 Helix-turn-helix, AraC type
IPR001005 SANT, DNA-binding
IPR001356 Homeobox
IPR001647 Transcriptional regulator, TetR-like, DNA-binding, bacterial/archaeal
IPR015010 Rap1 Myb
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Found in
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IPR000268 RNA polymerases, N/8kDa subunit
IPR003022 Transcription factor Otx2
IPR003025 Transcription factor Otx
IPR006695 Centromere protein Cenp-B, DNA-binding domain 1
IPR012738 Transcriptional regulator, DhaS
IPR015126 Mu DNA binding, I gamma subdomain
IPR017053 Response regulator, plant B-type
IPR017930 HTH transcriptional regulator, Myb-type, DNA-binding
IPR018060 Helix-turn-helix, AraC domain
IPR019915 Transcriptional regulator, pyrimidine utilisation, RutR
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Contains
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IPR000047 Helix-turn-helix motif, lambda-like repressor
IPR001827 Homeobox protein, antennapedia type, conserved site
IPR002197 Helix-turn-helix, Fis-type
IPR004906 Pogo transposase / Cenp-B / PDC2, subgroup, DNA-binding HTH domain
IPR014778 Myb, DNA-binding
IPR017970 Homeobox, conserved site
IPR020479 Homeobox, region
IPR020789 RNA polymerases, subunit N, zinc binding site
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GO Term annotation
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Process
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GO:0045449 regulation of transcription
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Function
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GO:0003677 DNA binding
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Homeodomain proteins are transcription factors that share a related DNA binding homeodomain [1]. The homeodomain was first identified in a number of Drosophila homeotic and segmentation proteins, but is now known to be well conserved in many other animals, including vertebrates. The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha helices, which make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions, which occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA. The first helix helps to stabilise the structure. Many proteins contain homeodomains, including Drosophila Engrailed, yeast mating type proteins, hepatocyte nuclear factor 1a and HOX proteins.
The homeodomain motif is very similar in sequence and structure to domains in a wide range of DNA-binding proteins, including recombinases, Myb proteins, GARP response regulators, human telomeric proteins (hTRF1), paired domain proteins (PAX), yeast RAP1, centromere-binding proteins CENP-B and ABP-1, transcriptional regulators (TyrR), AraC-type transcriptional activators, and tetracycline repressor-like proteins (TetR, QacR, YcdC) [2, 3, 4].
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Structural links
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SCOP:
a.35.1.7
,
a.4.1.1
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a.4.1.11
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a.4.1.12
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a.4.1.2
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a.4.1.3
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a.4.1.4
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a.4.1.6
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a.4.1.7
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a.4.1.8
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a.4.1.9
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a.4.11.1
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a.6.1.7
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b.82.4.1
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i.11.1.1
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i.8.1.1
,
j.92.1.1
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Interactions
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This domain has been experimentally proven to be involved in Protein:Protein interactions. Representative
data is shown with the following
example proteins:
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Publications
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1.
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Mannervik M.
Target genes of homeodomain proteins.
Bioessays 21 267-70 1999
[PubMed: 10377888]
http://dx.doi.org/10.1002/(SICI)1521-1878(199904)21:4<267::AID-BIES1>3.3.CO;2-3
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2.
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Hosoda K, Imamura A, Katoh E, Hatta T, Tachiki M, Yamada H, Mizuno T, Yamazaki T.
Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators.
Plant Cell 14 2015-29 2002
[PubMed: 12215502]
http://dx.doi.org/10.1105/tpc.002733
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3.
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Nishikawa T, Nagadoi A, Yoshimura S, Aimoto S, Nishimura Y.
Solution structure of the DNA-binding domain of human telomeric protein, hTRF1.
Structure 6 1057-65 1998
[PubMed: 9739097]
http://dx.doi.org/10.1016/S0969-2126(98)00106-3
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4.
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Kisker C, Hinrichs W, Tovar K, Hillen W, Saenger W.
The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance.
J. Mol. Biol. 247 260-80 1995
[PubMed: 7707374]
http://dx.doi.org/10.1006/jmbi.1994.0138
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Additional Reading
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Religa TL.
Comparison of multiple crystal structures with NMR data for engrailed homeodomain.
J. Biomol. NMR 40 2008 189-202
[PubMed: 18274703]
http://dx.doi.org/10.1007/s10858-008-9223-9
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Resch M, Striegl H, Henssler EM, Sevvana M, Egerer-Sieber C, Schiltz E, Hillen W, Muller YA.
A protein functional leap: how a single mutation reverses the function of the transcription regulator TetR.
Nucleic Acids Res. 36 2008 4390-401
[PubMed: 18587152]
http://dx.doi.org/10.1093/nar/gkn400
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Aleksandrov A, Schuldt L, Hinrichs W, Simonson T.
Tet repressor induction by tetracycline: a molecular dynamics, continuum electrostatics, and crystallographic study.
J. Mol. Biol. 378 2008 898-912
[PubMed: 18395746]
http://dx.doi.org/10.1016/j.jmb.2008.03.022
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Joshi R, Passner JM, Rohs R, Jain R, Sosinsky A, Crickmore MA, Jacob V, Aggarwal AK, Honig B, Mann RS.
Functional specificity of a Hox protein mediated by the recognition of minor groove structure.
Cell 131 2007 530-43
[PubMed: 17981120]
http://dx.doi.org/10.1016/j.cell.2007.09.024
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Hirata A, Klein BJ, Murakami KS.
The X-ray crystal structure of RNA polymerase from Archaea.
Nature 451 2008 851-4
[PubMed: 18235446]
http://dx.doi.org/10.1038/nature06530
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Ko S, Jun SH, Bae H, Byun JS, Han W, Park H, Yang SW, Park SY, Jeon YH, Cheong C, Kim WT, Lee W, Cho HS.
Structure of the DNA-binding domain of NgTRF1 reveals unique features of plant telomere-binding proteins.
Nucleic Acids Res. 36 2008 2739-55
[PubMed: 18367475]
http://dx.doi.org/10.1093/nar/gkn030
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